We have constructed (and continue to develop) a laser-based facility for time-resolved fluorescence spectroscopy of biomolecules. This facility provides rapid collection and analysis of luminescence data related to macromolecular size, flexibility, folding and structural fluctuations. This gives us insight into the structure and movements of proteins and membranes. The method is also sensitive enough to study nanogram quantities (100 fold more sensitive than nmr). Our main "time-correlated" fluorometer was utilized to study the folding and dynamics of many different proteins: interleukin-1-beta, a potent immunomodulator that is drawing interest in AIDS and cancer therapies; vl & v2, cloned fragments of the T-cell receptor "targeted" by HIV particles; TF3A, a DNA-binding protein whose zinc "fingers" control transcription; 'HApep', a protein fragment that the influenza virus uses to anchor to and fuse with our cell membranes; thioredoxin, an important cofactor for genetic processing; actin, actobindin and tubulin, structural elements in the "self-assembling scaffolding" of cells called cytoskeleton; arginase, a metabolic enzyme complex with manganese-controlled "switching", and several other proteins and membranes.